ArticleBMC biotechnology2018
Effects of substrate binding site residue substitutions of xynA from Bacillus amyloliquefaciens on substrate specificity.
Article in BMC biotechnology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Bioconversion of wild Ipomoea pes-caprae and Suaeda fruticosa biomass: a novel application of thermostable xylanase from Neobacillus sedimentimangrovi.BMC biotechnology · 2025Article
- Metagenomic mining unveils a novel GH130 enzyme with exclusive xylanase activity over a wide temperature and pH ranges.Journal of industrial microbiology & biotechnology · 2024Article
- Enhanced production of amyrin in Yarrowia lipolytica using a combinatorial protein and metabolic engineering approach.Microbial cell factories · 2022Article
- High-temperature behavior of hyperthermostable Thermotoga maritima xylanase XYN10B after designed and evolved mutations.Applied microbiology and biotechnology · 2022Article
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Authors and funding
7 authors.
Funding
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Abstract
backgroundThe aromatic residues of xylanase enzyme, W187, Y124, W144, Y128 and W63 of substrate binding pocket from Bacillus amyloliquefaciens were investigated for their role in substrate binding by homology modelling and sequence analysis. These residues are highly conserved and play an important role in substrate binding through steric hindrance. The substitution of these residues with alanine allows the enzyme to accommodate nonspecific substrates.
resultsWild type and mutated genes were cloned and overexpressed in BL21. Optimum pH and temperature of rBAxn exhibited pH 9.0 and 50 °C respectively and it was stable up to 215 h. Along with the physical properties of rBAxn, kinetic parameters (K
conclusionsThe site-specific single mutation, led to alteration in substrate specificity from xylan to CMC while in case of double mutant the substrate specificity was altered from xylan to CMC, FP and avicel, indicating the role of aromatic residues on substrate binding, catalytic process and overall catalytic efficiency.
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